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Gene Review

ARL3  -  ADP-ribosylation factor-like 3

Homo sapiens

Synonyms: ADP-ribosylation factor-like protein 3, ARFL3
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High impact information on ARL3


Biological context of ARL3

  • Two-hybrid screens of human cDNA libraries with dominant active mutants of human ARL1, ARL2, and ARL3 identified eight different but overlapping sets of binding partners [2].
  • CONCLUSION: The disturbed magnesium binding site and the independence of GDP coordination from the presence of Mg2+ separate ARL2 and ARL3 from Arf proteins [3].
  • Here we describe the methodologies that we have developed to analyze the interaction of RP2 with Arl3 and to investigate the effect of RP2 post-translational modifications on its subcellular and tissue localization [4].
  • We conclude that Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis [5].
  • Somewhat paradoxically, no phenotypes were observed Arl2 expression was knocked down or Arl3 activity was increased in HeLa cells [5].

Anatomical context of ARL3

  • These data suggest that RP2 functions in concert with Arl3 to link the cell membrane with the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery [1].
  • The presence of Arl3 in centrosomes, mitotic spindles, midzones, midbodies, and cilia are all supportive of roles in microtubule-dependent processes [5].
  • A number of human tumor cell lines expressed Arl3, as determined by immunoblotting with an Arl-specific antibody, raised against a peptide derived from the human Arl3 sequence [6].

Associations of ARL3 with chemical compounds

  • In contrast to ARF proteins, the Arl3 protein has reduced dependence on phospholipids and magnesium for guanine nucleotide exchange [6].
  • The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner [7].

Physical interactions of ARL3

  • It has been shown that RP2 can interact directly with Arl3 [4].

Other interactions of ARL3


Analytical, diagnostic and therapeutic context of ARL3


  1. Localization in the human retina of the X-linked retinitis pigmentosa protein RP2, its homologue cofactor C and the RP2 interacting protein Arl3. Grayson, C., Bartolini, F., Chapple, J.P., Willison, K.R., Bhamidipati, A., Lewis, S.A., Luthert, P.J., Hardcastle, A.J., Cowan, N.J., Cheetham, M.E. Hum. Mol. Genet. (2002) [Pubmed]
  2. ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins. Van Valkenburgh, H., Shern, J.F., Sharer, J.D., Zhu, X., Kahn, R.A. J. Biol. Chem. (2001) [Pubmed]
  3. Structural and biochemical properties show ARL3-GDP as a distinct GTP binding protein. Hillig, R.C., Hanzal-Bayer, M., Linari, M., Becker, J., Wittinghofer, A., Renault, L. Structure (2000) [Pubmed]
  4. Assay and functional analysis of the ARL3 effector RP2 involved in X-linked retinitis pigmentosa. Evans, R.J., Chapple, J.P., Grayson, C., Hardcastle, A.J., Cheetham, M.E. Meth. Enzymol. (2005) [Pubmed]
  5. Arl2 and Arl3 Regulate Different Microtubule-dependent Processes. Zhou, C., Cunningham, L., Marcus, A.I., Li, Y., Kahn, R.A. Mol. Biol. Cell (2006) [Pubmed]
  6. ADP-ribosylation factor (ARF)-like 3, a new member of the ARF family of GTP-binding proteins cloned from human and rat tissues. Cavenagh, M.M., Breiner, M., Schurmann, A., Rosenwald, A.G., Terui, T., Zhang, C., Randazzo, P.A., Adams, M., Joost, H.G., Kahn, R.A. J. Biol. Chem. (1994) [Pubmed]
  7. The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. Linari, M., Hanzal-Bayer, M., Becker, J. FEBS Lett. (1999) [Pubmed]
  8. Membrane traffic: Arl GTPases get a GRIP on the Golgi. Jackson, C.L. Curr. Biol. (2003) [Pubmed]
  9. Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Kühnel, K., Veltel, S., Schlichting, I., Wittinghofer, A. Structure (2006) [Pubmed]
  10. LdARL-3A, a Leishmania promastigote-specific ADP-ribosylation factor-like protein, is essential for flagellum integrity. Cuvillier, A., Redon, F., Antoine, J.C., Chardin, P., DeVos, T., Merlin, G. J. Cell. Sci. (2000) [Pubmed]
  11. Identification of genes differentially expressed in V79 cells grown as multicell spheroids. Oloumi, A., Lam, W., Banáth, J.P., Olive, P.L. Int. J. Radiat. Biol. (2002) [Pubmed]
  12. Assignment of the human ADP-ribosylation factor-like 3 (ARL3) gene to chromosome 10 band q23.3 by radiation hybrid mapping. Kim, H.S. Cytogenet. Cell Genet. (1998) [Pubmed]
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